Abstract
The treatment of bacterial diseases has become a serious problem in clinical medicine in large part because of antibiotic resistance. One way bacteria have increased resistance to drugs is the overexpression of multidrug efflux pumps, exemplified by AcrAB‐TolC, a group of three proteins that span both the inner and outer membranes of E. coli. AcrAB‐TolC transports a wide range of foreign compounds and a broad spectrum of antibiotics. AcrB forms a homo‐trimeric structure that uses cyclical conformational changes powered by ATP to transport foreign compounds into the TolC pore which eventually expels the compounds from the bacteria. The role of AcrA is less defined, perhaps providing structural support to AcrB. The Madison West High School SMART Team (Students Modeling A Research Topic) modeled the interactions between AcrB and associated proteins in the E. coli pump using 3D printing technology to further study the mechanisms of bacterial drug efflux, as well as gain a better understanding of other drug efflux transport mechanisms, such as that used by P‐glycoprotein, which is important in cancer biology and human resistance to chemotherapeutics. The study of the detailed structures of AcrAB‐TolC may be of paramount importance in the development of novel pharmaceuticals against bacterial infections. Supported by grants from NIH‐SEPA and NIH‐CTSA.
Published Version
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